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Adenylate Kinase 2 Human Recombinant ( AK2 Human )
DescriptionAK2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 259 amino acids and having a molecular mass of 28.6 kDa. AK2 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary
Data sheet
| Formulation | AK2 solution containing 20mM Tris pH-7.5, 5mM DTT and 20% glycerol. |
| Purity | Greater than 95.0% as determined by SDS-PAGE. |
| Description | AK2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 259 amino acids and having a molecular mass of 28.6 kDa. AK2 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques. |
| Protein Background | Adenylate kinases play a role in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate groups among adenine nucleotides. There are 3 types of adenylate kinase isozymes, AK1, AK2, and AK3 in vertebrates. Expression of these isozymes are tissue-specific and developmentally regulated. AK2 is localized in the mitochondrial intermembrane space and is involved in apoptosis. AK2 is mutated in individuals with reticular dysgenesis. |
| Expression host | Escherichia Coli. |
| Synonyms | ADK2, AK-2, Adenylate kinase isoenzyme 2 mitochondrial, ATP-AMP transphosphorylase 2, adenylate kinase 2. |
| Reagent Appearance | Sterile filtered colorless solution. |
| Stability | AK2 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles. |
| Amino acid sequence | MGSSHHHHHH SSGLVPRGSH MAPSVPAAEP EYPKGIRAVL LGPPGAGKGTQAPRLAENFC VCHLATGDML RAMVASGSEL GKKLKATMDA GKLVSDEMVV ELIEKNLETP LCKNGFLLDG FPRTVRQAEM LDDLMEKRKE KLDSVIEFSIPDSLLIRRIT GRLIHPKSGR SYHEEFNPPK EPMKDDITGE PLIRRSDDNE KALKIRLQAY HTQTTPLIEY YRKRGIHSAI DASQTPDVVF ASILAAFSKA TCKDLVMFI. |
| Biological Activity | Specific activity: > 1.5 units/ml. One unit will convert 2.0 umoles of ADP to ATP + AMP per minute at pH 7.5 at 25C. |